1.C.125.  The Pore-forming Stonustoxin (Stonustoxin) Family 

Stonustoxin is lethal towards mice and induces hemolytic activities due to its ability to form pores in the cell membrane (Poh et al. 1991; Chen et al. 1997). It elicits potent hypotension which is endothelium-dependent and appears to be mediated via the nitric oxide pathway. I activates potassium channels, displays edema-inducing activities, increases vascular permeability and induces endothelium-dependent vasorelaxation of isolated rat aorta while inducing platelet aggregation.  It is myotoxic and interferes irreversibly with neuromuscular function (Low et al. 1994). It is derived from the venom of the Scorpaena plumieri fish which have been analyzed by proteomic approaches (Borges et al. 2018).

 


 

References:

Borges, M.H., F. Andrich, P.H. Lemos, T.G. Soares, T.N. Menezes, F.V. Campos, L.X. Neves, W. Castro-Borges, and S.G. Figueiredo. (2018). Combined proteomic and functional analysis reveals rich sources of protein diversity in skin mucus and venom from the Scorpaena plumieri fish. J Proteomics 187: 200-211.

Chen, D., R.M. Kini, R. Yuen, and H.E. Khoo. (1997). Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues. Biochem. J. 325(Pt3): 685-691.

Low, K.S., M.C. Gwee, R. Yuen, P. Gopalakrishnakone, and H.E. Khoo. (1994). Stonustoxin: effects on neuromuscular function in vitro and in vivo. Toxicon 32: 573-581.

Poh, C.H., R. Yuen, H.E. Khoo, M. Chung, M. Gwee, and P. Gopalakrishnakone. (1991). Purification and partial characterization of stonustoxin (lethal factor) from Synanceja horrida venom. Comp Biochem Physiol B 99: 793-798.

Examples:

TC#NameOrganismal TypeExample
1.C.125.1.1

Two component stonustoxin with alpha and beta subunits, of 703 aas (α-toxin) and 700 aas (β-toxin). See family descriiption for description and references. The two subunits are 47% identical.

Stonustoxin of Synanceia horrida (Estuarine stonefish) (Scorpaena horrida)

 
1.C.125.1.2

Cytotoxin with two subunits, α (703 aas) and β (698 aas) (Borges et al. 2018).

Cytotoxin of Scorpaenopsis oxycephala

 
1.C.125.1.3

Cytotoxin with three subunits, α (586 aas), β (585 aas) and γ (583 aas).

Cytotoxin of Dendrochirus xebra

 
1.C.125.1.4

Patoxin with two subunits, α of 699 aas and β of 698 aas (Borges et al. 2018).

Patoxin of Pterois antennata